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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

12 Issues per year


IMPACT FACTOR 2016: 3.273

CiteScore 2016: 3.01

SCImago Journal Rank (SJR) 2016: 1.679
Source Normalized Impact per Paper (SNIP) 2016: 0.800

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1437-4315
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Volume 389, Issue 9 (Sep 2008)

Issues

Some assembly required: dedicated chaperones in eukaryotic proteasome biogenesis

Andrew R. Kusmierczyk
  • 1Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA
  • Other articles by this author:
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/ Mark Hochstrasser
  • 2Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2008-08-19 | DOI: https://doi.org/10.1515/BC.2008.130

Abstract

The 26S proteasome is the key eukaryotic protease responsible for the degradation of intracellular proteins. Protein degradation by the 26S proteasome plays important roles in numerous cellular processes, including the cell cycle, differentiation, apoptosis, and the removal of damaged or misfolded proteins. How this 2.5-MDa complex, composed of at least 32 different polypeptides, is assembled in the first place is not well understood. However, it has become evident that this complicated task is facilitated by a framework of protein factors that chaperone the nascent proteasome through its various stages of assembly. We review here the known proteasome-specific assembly factors, most only recently discovered, and describe their potential roles in proteasome assembly, with an emphasis on the many remaining unanswered questions about this intricate process of assisted self-assembly.

Keywords: assembly factor; maturation; protein complex; yeast

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Published Online: 2008-08-19

Published in Print: 2008-09-01


Citation Information: Biological Chemistry, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2008.130.

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